4mc8
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Hedycaryol synthase in complex with HEPES== | |
| + | <StructureSection load='4mc8' size='340' side='right'caption='[[4mc8]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_setae_KM-6054 Kitasatospora setae KM-6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MC8 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mc8 OCA], [https://pdbe.org/4mc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mc8 RCSB], [https://www.ebi.ac.uk/pdbsum/4mc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mc8 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HCS_KITSK HCS_KITSK] Catalyzes the conversion of (2E,6E)-farnesyl diphosphate (FPP) into (2Z,6E)-hedycaryol via a 1,11-cyclization.<ref>PMID:24399794</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The biosynthesis of terpenes is catalysed by class I and II terpene cyclases. Here we present structural data from a class I hedycaryol synthase in complex with nerolidol, serving as a surrogate for the reaction intermediate nerolidyl diphosphate. This prefolded ligand allows mapping of the active site and hence the identification of a key carbonyl oxygen of Val179, a highly conserved helix break (G1/2) and its corresponding helix dipole. Stabilising the carbocation at the substrate's C1 position, these elements act in concert to catalyse the 1,10 ring closure, thereby exclusively generating the anti-Markovnikov product. The delineation of a general mechanistic scaffold was confirmed by site-specific mutations. This work serves as a basis for understanding carbocation chemistry in enzymatic reactions and should contribute to future application of these enzymes in organic synthesis. | ||
| - | + | Hedycaryol synthase in complex with nerolidol reveals terpene cyclase mechanism.,Baer P, Rabe P, Citron CA, de Oliveira Mann CC, Kaufmann N, Groll M, Dickschat JS Chembiochem. 2014 Jan 24;15(2):213-6. doi: 10.1002/cbic.201300708. Epub 2014 Jan , 7. PMID:24399794<ref>PMID:24399794</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4mc8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Kitasatospora setae KM-6054]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Baer P]] | ||
| + | [[Category: Cirton C]] | ||
| + | [[Category: Dickschat J]] | ||
| + | [[Category: Groll M]] | ||
| + | [[Category: Kaufmann N]] | ||
| + | [[Category: Oliveira Mann C]] | ||
| + | [[Category: Rabe P]] | ||
Current revision
Hedycaryol synthase in complex with HEPES
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